X-ray crystallography and solution NMR are mature fields that provide powerful tools for macromolecular structure determination. Nonetheless, structural characterization still poses a formidable challenge for many targets. For example, the diverse conformational transitions explored by unsynchronized populations of multi-protein complexes can confound bulk analytical approaches. CryoEM has the advantage of single-molecule imaging; however computational averaging is required for recovery of high-resolution structure. For samples exhibiting conformational heterogeneity, poor signal-to-noise under low-dose imaging leads to errors during class assignment of particles, thereby compromising effective resolution of reconstructions. Therefore a great need persists for novel technologies that can complement standard structural-biology approaches. A valuable source of such additional data is the long-range distance restraint, as sets of these considerably simplify the conformational search space for computational methods of structure determination. In the short term, long-range distance restraints can be used to refine models of docking of well-defined subunits, derived from previously determined x-ray or NMR studies, into larger complexes. In the longer term, these data could be used as the major source of experimental restraints for guiding de novo computational fold prediction. Single-molecule FRET is a promising approach for producing long-range distance restraints, however it currently requires extensive cysteine engineering along with complex instrumentation and analysis to obtain even a modest number of these distances. Thus no current methods exist for low-cost, high-throughput collection of long-range distance restraints at a single-molecule level.